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Amino acid substitutions in mitochondrial ATPase subunit 6 of Saccharomyces cerevisiae leading to oligomycin resistance
Author(s) -
John Ulrik P.,
Nagley Phillip
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80016-3
Subject(s) - oligomycin , protein subunit , saccharomyces cerevisiae , amino acid , inner mitochondrial membrane , biochemistry , biology , mutant , mitochondrion , peptide sequence , atpase , mitochondrial carrier , gene , bacterial outer membrane , enzyme , escherichia coli
The amino acid substitutions in subunit 6 of the mitochondrial ATPase complex have been determined for 4 oligomycin resistant mutants of Saccharomyces cerevisiae . The data were obtained for each mutant by nucleotide sequence analysis of the mitochondrial oli2 gene. Amino acid substitutions conferring oligomycin resistance in subunit 6 are located in two conserved regions that are thought to form domains which span the inner mitochondrial membrane. The disposition of these amino acid substitutions is consistent with the view that these two membrane‐spanning domains interact structurally and functionally with the DCCD‐binding proteolipid subunit 9 in the F 0 ‐sector.